(2-Aminoethyl)phosphonic acid

A new amido phosphonate derivative of carboxymethylcellulose with an osteogenic activity and which is capable of interacting with any Ti surface.[Pubmed:20740601]

J Biomed Mater Res A. 2010 Oct;95(1):58-67.

A new phosphonate derivative of carboxymethylcellulose (CMC) was recently synthesized (CMCAPh). The phosphonate polysaccharide was obtained by using a carbodiimide-like activating agent for carboxylic groups and 2-aminoethyl-phosphonic acid to create an amide bond between the amine of the phosphonate agent and the carboxylic acids of CMC. The polymer was characterized by (31)P NMR, FT-IR, and potentiometric titration. CMCAPh showed different properties from CMC and its amidated derivative polymer CMCA. The behavior in solution of CMCAPh polymer towards normal human osteoblasts (NHOst) was studied in vitro, monitoring the cell proliferation, cell differentiation, and osteogenic activity and was then compared with the amidic derivative of carboxymethylcellulose (CMCA). Furthermore, CMCAPh was used to coat titania disks with the aim of increasing the osteogenic activity of implant surfaces. The polymer film on the titania surface was characterized by AFM and TOF-SIMS analysis. An ATR FT-IR study was carried out to evaluate the polymer bonding mode onto the titanium surface. Osteoblast morphology was evaluated by SEM. Adhesion analysis of NHOst demonstrated a better adhesion on the titanium surface coated with CMCAPh than on the bare titanium surface.

2-Aminoethylphosphonic acid as an indicator of Tetrahymena pyriformis W growth in protein-quality evaluation assay.[Pubmed:96851]

Br J Nutr. 1978 Jul;40(1):83-90.

1. The concentration of 2-aminoethylphosphonic acid (AEP) in 96 h cultures of Tetrahymena pyriformis W was studied in order to apply it as an indicator in the assay of the relative nutritive value (RNV; protozoa population with test protein:protozoa population with whole-egg powder) of protein. Foodstuffs and food mixtures of different protein contents and qualities were used as test samples. 2. RNV values based on AEP determination (RNVAEP) were compared with corresponding values calculated from protozoa counts (RNVpc), as well as with biological value (BV) and net protein utilization (NPU) of the same proteins assayed on rats. 3. Both for foodstuffs and food mixtures highly significant correlations were found between RNVAEP and RNVpc, RNVAEP and both BV and NPU, and RNVpc and both BV and NPU. 4. AEP content in the protozoal suspension was preferred to cell count as a measure of growth response, since it took into account large differences in cell dimensions that were observed between cultures grown with different test proteins.

Protein binding to amphoteric polymer brushes grafted onto a porous hollow-fiber membrane.[Pubmed:17918859]

Biotechnol Prog. 2007 Nov-Dec;23(6):1425-30.

Three kinds of ampholites, i.e., 3-aminopropionic acid (NH2C2H4COOH), (2-Aminoethyl)phosphonic acid (NH2C2H4PO3H2), and 2-aminoethane-1-sulfonic acid (NH2C2H4SO3H), were introduced into an epoxy group-containing polymer brush grafted onto a porous hollow-fiber membrane with a porosity of 70% and pore size of 0.36 microm. The amphoteric group density of the hollow-fiber ranged from 0.50 to 0.72 mmol/g. Three kinds of proteins, i.e., lactoferrin (Lf), cytochrome c (Cyt c), and lysozyme (Ly), were captured by the amphoteric polymer brush during the permeation of the protein solution across the ampholite-immobilized porous hollow-fiber membrane. Multilayer binding of the protein to the amphoteric polymer brush, with a degree of multilayer binding of 3.3, 8.6, and 15 for Lf, Cyt c, and Ly, respectively, with the (2-Aminoethyl)phosphonic acid-immobilized porous hollow-fiber membrane, was demonstrated with a negligible diffusional mass-transfer resistance of the protein to the ampholite immobilized. The 2-aminoethane-1-sulfonic acid-immobilized porous hollow-fiber membrane exhibited the lowest initial flux of the protein solution, 0.41 m/h at a transmembrane pressure of 0.1 MPa and 298 K, and the highest equilibrium binding capacity of the protein, e.g., 130 mg/g for lysozyme. Extension and shrinkage of the amphoteric polymer brushes were observed during the binding and elution of the proteins.